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Database: UniProt
Entry: A0A1K1RMH3_9BACT
LinkDB: A0A1K1RMH3_9BACT
Original site: A0A1K1RMH3_9BACT 
ID   A0A1K1RMH3_9BACT        Unreviewed;      1467 AA.
AC   A0A1K1RMH3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05661012_03977 {ECO:0000313|EMBL:SFW73222.1};
OS   Chitinophaga sancti.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW73222.1, ECO:0000313|Proteomes:UP000183788};
RN   [1] {ECO:0000313|EMBL:SFW73222.1, ECO:0000313|Proteomes:UP000183788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 784 {ECO:0000313|EMBL:SFW73222.1,
RC   ECO:0000313|Proteomes:UP000183788};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; FPIZ01000013; SFW73222.1; -; Genomic_DNA.
DR   STRING; 1004.SAMN05661012_03977; -.
DR   Proteomes; UP000183788; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF07494; Reg_prop; 6.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1467
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013199219"
FT   TRANSMEM        923..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          969..1178
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1216..1331
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1363..1462
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   REGION          25..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1264
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1467 AA;  165275 MW;  EB86602D207BEFF7 CRC64;
     MRLQQYFHLL CGLLLPSLTG LSILSASPVD TNPEKKTRTN TVRETQAGTA RETHTGAASK
     TYTNTSREIH TSSPRETHTG TANKTYTNPP GEIHTSSRTN TDPSANIRLE QLTTYDGLSQ
     NTVRCLLQDK KGFIWVGTLN GLNRYDGRKF TVYRTNTGIT QPISDNRIRS LYEDKKGIIW
     VKTAEGHYHC FDPGKETFIN IIPDSADLTY DHLFETTKGV WLYSKTNGCL HNGRHYNLGS
     VHFIFEDSRH TEWIGTDKNL YQLDKQGNAI PLYEGNFIKA ITKAEQLYFI KKQGILIHDL
     HTNKCTFNDP LPGTILTDAA ILPNNRILLG TQQDGLKIAD LQNNRLIPTT RLFGEDIPGH
     IDIETDQDAG IWVNNHTGNV WYLDPAQAFS QRITLIPASV MKVIDDCRFA FAADHKGKVW
     ITTYGGGLYC FDKTNRQLQR FVYDPDNPNG LSTNYLLSVI ADRAGLIWVG AEHTGLQKLT
     PQSLHVTHIF PEAQTPERYA ANGVKTIFED SYKRIWVSTR NGALYLYNDH LEKNRSLDHL
     LPGQCANIYC MTEDARGYLW IGTKGDGVYI VHRDSLQQKA RHFLLPSRDN RLVYTIMQDR
     QQRMWVGTFG SGLYLATYKG GNQLEWQNFF HDGVNPVYIR CLLQDQHNQL WAGTNNGLLV
     FNPEHLLAGN NDITTYQAGL GSNEIKSLCE DHKGRIWIGT TGGGFSRFVP QKKTFINYTT
     EQGLSHDVVN SMLEDAQGNL WVSTENGLTR FNPEKSTFEV FYFANNPLGN LFSEGACFRR
     ENGQLLWGSL NGFYSFFPGQ LKNGNADAPV LLTGLSVAGN PVVLEESIST ARSITLEPGQ
     KVFSISFASL ALRNPQQNKY TYILENYEDE WNAPSSYNVA TYRNLPPGKY TFKVRGTNDD
     GSWSKHEARI QITVLPPFWR SNVAIMLSLA LIIGMVMCVI VINRRIHRLQ HAVTLEKELT
     EYKLNFFTDI SHEFRTPLSL IVSAMEQLIP GKQSGNKHLH IMQRQVAHLM RLADQLLDFR
     KIQHKKLQLQ VQETEMIQFI QDICNGFTDL AAQKQITLSF RANVDACMAW VDQGKLDKIL
     YNLLSNAHKF TPAGGKIDLL VHIDHQLTIK VVDNGIAISA EKQHMVFQRF TQLNFSPTGT
     GLGLSLTKEL VTLHKGTISF ENNADAGVTF TVNLPVHKLA YVADEIVEQT ICKAPVLPFI
     DDTDTAAIVA PSSRYSVLII EDNPDISAYL ATTLSRYFHI YTAANGREGL EQAIAQSPDL
     IVCDVMLPEM NGLEITHKIR SEFQTCHIPV ILLTALSSGE HQLQGIDAGA DAYITKPFST
     RFLLTSIIRI IEQREKIRKR FANDPGFFAV HISENEADQQ FLEKINMIIE KNLDNAQFSV
     DDFALAMKMG RTLFYKKVKG LTGYSPNEYI RLVRVKKAAE LLNTGEYTVA EVAYKVGMND
     PFYFSKCFKT QFGVPPSVHL KKVKAAG
//
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